1zwf

STRUCTURE OF N-TERMINAL ACETYLATED HUMAN PARATHYROID HORMONE, NMR, 10 STRUCTURES

Method: SOLUTION NMR Dmax: 38.5 Å Quality: REASONABLE

1. Protein Identity and Related Structures Protein Identity & Related Structures

PARATHYROID HORMONE

Homo sapiens

UniProt P01270

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 35–68 Fragment:4 - 37 Mutation:N-TERMINAL ACETYLATED Non-standard monomer:Yes (specific site not provided by mmCIF) No other associated polymer SOLUTION NMR mmCIF provides none of the parsed experimental conditions Resolution not provided

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

25 other PDB entries and 26 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PTHY_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–35; UniProt 35–68

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 1zwf

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1zwf
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1zwf
Deposition date deposition_date1996-06-17
Structure title titleSTRUCTURE OF N-TERMINAL ACETYLATED HUMAN PARATHYROID HORMONE, NMR, 10 STRUCTURES
Keywords keywordsHORMONE, DISEASE MUTATION; HORMONE
Experimental Method methodSOLUTION NMR

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier10.97
Radius of gyration Rg (electron density) rg_electron10.80
Forward intensity I(0) i026452400.00
Molecular weight molecular_weight41719.0 kDa
Excluded volume excluded_volume52449 ų
Envelope volume envelope_volume16637 ų
Hydration-shell volume shell_volume10935 ų
Envelope diameter envelope_diameter41.9
Shell Rg shell_rg18.70
Envelope Rg envelope_rg13.34
Shape Rg shape_rg10.73
Total Rg total_rg11.68
Total atoms total_atoms5920
Residues n_residues340
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax38.5
Rg (real space) rg_real10.99
Rg uncertainty (real space) rg_real_error0.34
I(0) (real space) i0_real2.6450e+07
I(0) uncertainty (real space) i0_real_error2.5720e+05
Rg (reciprocal space) rg_reciprocal10.99
I(0) (reciprocal space) i0_reciprocal26450000.0000
Solution quality estimate total_estimate0.6228
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary14.2
Skewness Skewness skewness0.267
Kurtosis Kurtosis kurtosis-0.358
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha21200.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.826; Stabil: 1.000; Sysdev: 0.256; Positv: 1.000; Valcen: 0.846; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1zwfa_
Class classj — Peptides
Fold Fold foldj.15 — Parathyroid hormone fragments (residues between 1 and 39)
Superfamily Superfamily superfamilyj.15.1 — Parathyroid hormone fragments (residues between 1 and 39)
Family Family familyj.15.1.1 — Parathyroid hormone fragments (residues between 1 and 39)

8. Citations (1)

9. Files and Curves (10)